5MTW
Mycobacterium tuberculosis Rv1957 SecB-like chaperone in complex with a ChAD peptide from Rv1956 HigA1 antitoxin
Summary for 5MTW
| Entry DOI | 10.2210/pdb5mtw/pdb |
| Descriptor | SecB-like chaperone Rv1957, Antitoxin HigA1, DIMETHYL SULFOXIDE, ... (5 entities in total) |
| Functional Keywords | toxin-antitoxin-chaperone system, complex, chaperone |
| Biological source | Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) More |
| Total number of polymer chains | 7 |
| Total formula weight | 86687.22 |
| Authors | Guillet, V.,Mourey, L. (deposition date: 2017-01-10, release date: 2018-10-24, Last modification date: 2024-01-17) |
| Primary citation | Guillet, V.,Bordes, P.,Bon, C.,Marcoux, J.,Gervais, V.,Sala, A.J.,Dos Reis, S.,Slama, N.,Mares-Mejia, I.,Cirinesi, A.M.,Maveyraud, L.,Genevaux, P.,Mourey, L. Structural insights into chaperone addiction of toxin-antitoxin systems. Nat Commun, 10:782-782, 2019 Cited by PubMed Abstract: SecB chaperones assist protein export by binding both unfolded proteins and the SecA motor. Certain SecB homologs can also control toxin-antitoxin (TA) systems known to modulate bacterial growth in response to stress. In such TA-chaperone (TAC) systems, SecB assists the folding and prevents degradation of the antitoxin, thus facilitating toxin inhibition. Chaperone dependency is conferred by a C-terminal extension in the antitoxin known as chaperone addiction (ChAD) sequence, which makes the antitoxin aggregation-prone and prevents toxin inhibition. Using TAC of Mycobacterium tuberculosis, we present the structure of a SecB-like chaperone bound to its ChAD peptide. We find differences in the binding interfaces when compared to SecB-SecA or SecB-preprotein complexes, and show that the antitoxin can reach a functional form while bound to the chaperone. This work reveals how chaperones can use discrete surface binding regions to accommodate different clients or partners and thereby expand their substrate repertoire and functions. PubMed: 30770830DOI: 10.1038/s41467-019-08747-4 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.84 Å) |
Structure validation
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